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	Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism
	Fu, Xinmiao ; Chang, Zengyi
	2010-05-11 ; 2010-05-11
关键词	chaperone small heat shock protein Hsp16.3 N-terminal region bis-ANS CHAPERONE-LIKE ACTIVITY ALPHA-CRYSTALLIN 1,1'-BI(4-ANILINO)NAPHTHALENE-5,5'-DISULFONIC ACID MOLECULAR CHAPERONE DISSOCIATION EVOLUTION Biochemistry & Molecular Biology Biophysics
中文摘要	Small heat shock proteins (sHSPs), as one important subclass of molecular chaperones, are able to specifically bind to denatured substrate proteins rather than to native proteins, of which their substrate-binding sites are far from clear. Our previous study showed an overlapping nature of the sites for both hydrophobic probe 1,1'-Bi(4-anilino)naphthalene-5,5'-disulfonic acid (bis-ANS) binding and substrate binding in Mycobacterium tuberculosis Hsp 16.3 [X. Fu, H. Zhang, X. Zhang, Y. Cao, W. Jiao, C. Liu, Y. Song, A. Abulimiti, Z. Chang, A dual role for the N-terminal region of M. tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins, J. Biol. Chem. 280 (2005) 6337-6348]. In this work, two bis-ANS binding sites in Hsp16.3 were identified by a combined use of reverse phase HPLC, mass spectroscopy and N-terminal protein sequencing. One site is in the N-terminal region and the other one in the N-terminus of alpha-crystallin domain, both of which are similar to those identified so far in sHSPs. However, accumulating data suggest that these two sites differentially function in binding substrate proteins. With regard to this difference, we proposed a two-step mechanism by which Hsp16.3 binds substrate proteins, i.e., substrate proteins are recognized and initially captured by the N-terminal region that is exposed in the dissociated Hsp 16.3 oligomers, and then the captured substrate proteins are further stabilized in the complex by the subsequent binding of the N-terminus of alpha-crystallin domain. (c) 2006 Elsevier Inc. All rights reserved.
语种	英语 ; 英语
出版者	ACADEMIC PRESS INC ELSEVIER SCIENCE ; SAN DIEGO ; 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
内容类型	期刊论文
源URL	[http://hdl.handle.net/123456789/26640]
专题	清华大学
推荐引用方式 GB/T 7714	Fu, Xinmiao,Chang, Zengyi. Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism[J],2010, 2010.
APA	Fu, Xinmiao,&Chang, Zengyi.(2010).Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism..
MLA	Fu, Xinmiao,et al."Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism".(2010).

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